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A three‐step purification of human α 1 ‐acid glycoprotein
Author(s) -
Laurent Philippe,
Miribel Laurent,
Bienvenu Jacques,
Vallve Charles,
Arnaud Philippe
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80210-0
Subject(s) - affinity chromatography , isoelectric focusing , chromatography , chemistry , lectin , glycoprotein , affinity electrophoresis , isoelectric point , orosomucoid , electrophoresis , yield (engineering) , biochemistry , enzyme , materials science , metallurgy
α 1 ‐Acid glycoprotein (AGP) was purified to homogeneity by a 3‐step procedure using pseudo‐ligand affinity chromatography on immobilized Cibacron blue F3GA, Procion red HE3B, and preparative column isoelectric focusing. The overall yield of the combined techniques was 88%. Analysis of the purified AGP by lectin affinity chromatography on immobilized Con A and immunoaffinoelectrophoresis indicated that the most acidic form did not interact with the lectin, while the two more basic fractions possessed different affinities for Con A. In addition, 3 different populations of AGP were clearly separated by Con A affinity chromatography.